The 2-oxoacid dehydrogenase multienzyme complex of Haloferax volcanii

D M Al-Mailem, D W Hough, M J Danson

Research output: Contribution to journalArticle

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Abstract

Those aerobic archaea whose genomes have been sequenced possess four adjacent genes that, by sequence comparisons with bacteria and eukarya, appear to encode the component enzymes of a 2-oxoacid dehydrogenase multienzyme complex. However, no catalytic activity of any such complex has ever been detected in the archaea. In Thermoplasma acidophilum, evidence has been presented that the heterologously expressed recombinant enzyme possesses activity with the branched chain 2-oxoacids and, to a lesser extent, with pyruvate. In the current paper, we demonstrate that in Haloferax volcanii the four genes are transcribed as an operon in vivo. However, no functional complex or individual enzyme, except for the dihydrolipoamide dehydrogenase component, could be detected in this halophile grown on a variety of carbon sources. Dihydrolipoamide dehydrogenase is present at low catalytic activities, the level of which is increased three to fourfold when Haloferax volcanii is grown on the branched-chain amino acids valine, leucine and isoleucine.
Original languageEnglish
Pages (from-to)89-96
Number of pages8
JournalExtremophiles
Volume12
Issue number1
DOIs
Publication statusPublished - 2008

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Multienzyme Complexes
Haloferax volcanii
Dihydrolipoamide Dehydrogenase
Keto Acids
Archaea
Enzymes
Thermoplasma
Branched Chain Amino Acids
Isoleucine
Valine
Operon
Eukaryota
Pyruvic Acid
Leucine
Genes
Oxidoreductases
Carbon
Genome
Bacteria
Haloferax volcanii 2-oxoacid dehydrogenase complex

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The 2-oxoacid dehydrogenase multienzyme complex of Haloferax volcanii. / Al-Mailem, D M; Hough, D W; Danson, M J.

In: Extremophiles, Vol. 12, No. 1, 2008, p. 89-96.

Research output: Contribution to journalArticle

Al-Mailem, D M ; Hough, D W ; Danson, M J. / The 2-oxoacid dehydrogenase multienzyme complex of Haloferax volcanii. In: Extremophiles. 2008 ; Vol. 12, No. 1. pp. 89-96.
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